Transmitted drug resistance of HIV-1 strains among individuals attending voluntary counselling and testing in Taiwan.
PMID: 26404079
2016
The Journal of antimicrobial chemotherapy
Abstract: Among the seven major integrase mutations (T66I, E92Q, G140S, Y143C/H/R, S147G, Q148H/K/R and N155H), only one strain harbouring the Q148R mutation was detected.
Drug Susceptibility and Viral Fitness of HIV-1 with Integrase Strand Transfer Inhibitor Resistance Substitution Q148R or N155H in Combination with Nucleoside/Nucleotide Reverse Transcriptase Inhibitor Resistance Substitutions.
PMID: 26574015
2016
Antimicrobial agents and chemotherapy
Abstract: In clinical trials of coformulated elvitegravir (EVG), cobicistat (COBI), emtricitabine (FTC), and tenofovir disoproxil fumarate (TDF), emergent drug resistance predominantly involved the FTC resistance substitution M184V/I in reverse transcriptase (RT), with or without the tenofovir (TFV) resistance substitution K65R, accompanied by a primary EVG resistance substitution (E92Q, N155H, or Q148R) in integrase (IN).
Abstract: We previously reported that the RT-K65R, RT-M184V, and IN-
Effect on HIV-1 viral replication capacity of DTG-resistance mutations in NRTI/NNRTI resistant viruses.
Introduction: The absence of compensatory secondary mutations for R263K is also consistent with the observation that many major RAL- and EVG-resistance substitutions such as G140S, Q148R, E92Q, N155H
Discussion: Compared to WT virus, the R263K substitution as well as some other major mutations E92Q, Q148R and N155H, reported in the RAL- and/or EVG-resistance pathways, can emerge from a single nucleotide change in most HIV-1 strains.
Discussion: For example, N155H virus caused sixfold and fivefold decreases in susceptibility to RAL and EVG and E92Q conferred more than a 50-fold decrease in EVG susceptibility.
Prevalence of Integrase Strand Transfer Inhibitors (INSTI) Resistance Mutations in Taiwan.
Method: Besides these three major mutations, the integrase substitutions with a Stanford HIVdb score 10 to at least one INSTI were included, such as H51Y, T66A/I/K, L74M, E92G/Q/V, Q95K, T97A, F121Y, E138A/K, G140S/C/A, Y143G/K/S/A, P145S, Q146P, S147G, V151A/L, S153F/Y, N155S/T,
Antiviral Activity of Bictegravir (GS-9883), a Novel Potent HIV-1 Integrase Strand Transfer Inhibitor with an Improved Resistance Profile.
PMID: 27645238
2016
Antimicrobial agents and chemotherapy
Figure: Primary INSTI resistance mutations are T66I/A/K, E92Q/G, T97A, Y143C/H/R, S147G, Q148H/K/R, and N155H, and other INSTI resistance mutations are H51Y, L68I/V, V72A/N/T, L74M, Q95K/R, F121C/Y, A128T, E138A/K, G140A/C/S, P145S, PMID: 26311843
2015
The Journal of antimicrobial chemotherapy
Introduction: Three genotypic resistance pathways were identified: N155H (+-E92Q), Q148H/R/K (+-G140S) and Y143R (+-T97A).
Method: Major RAMs comprised T66A/I/K, E92Q/G/V, F121Y, Table: E92Q
Discussion: Consistent with available data, there was a strong preferential association of N155H with E92Q, Y143H/R/C with T97A, and G140S/A with Q148H/R/K.
[Resistance profile and genetic barrier of dolutegravir].
PMID: 25858608
2015
Enfermedades infecciosas y microbiologia clinica
Abstract: Dolutegravir displays in vitro activity against mutant HIV-1 harboring any isolated resistance mutations selected during failures to raltegravir or elvitegravir (Y143C/H/, N155H, Q148H/K/R, E92G/Q, T66A/I/K, T97A, E138A/K, G140A/S).
Influence of Drug Resistance Mutations on the Activity of HIV-1 Subtypes A and B Integrases: a Comparative Study.
Introduction: We characterized the catalytic activity of INA and its variants containing two major combinations of RALand EVG-resistance mutations: E92Q, V151I, N155H, G163R, L74M (mutant 1), and Q148K, E138K, G140S (mutant 2) .
Resistance against Integrase Strand Transfer Inhibitors and Relevance to HIV Persistence.
Introduction: Under such circumstances, extensive genotypic characterisation of resistant strains from two large clinical studies, i.e., Studies 102 and 103, revealed the emergence of the T66I, E92Q, T97A, Q148R and N155H resistance mutations in integrase, mostly in combination with the M184I/V substitutions in RT.
Table: E92E/Q
Table: E92Q
In vitro activity of dolutegravir against wild-type and integrase inhibitor-resistant HIV-2.
Abstract: Integrase substitutions E92Q, Y143C, E92Q + Y143C, and Q148R conferred relatively low levels of resistance to dolutegravir in HIV-2ROD9 (2- to 6-fold), but Q148K, E92Q + N155H, T97A + N155H and
Abstract: In contrast, HIV-1NL4-3 mutants E92Q + N155H, G140S + Q148R, and T97A + Y143C showed 2-fold, 4-fold, and no increase in EC50, respectively, relative to the parental strain.